PubMed:14681236
Annnotations
PubMed_ArguminSci
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 184-383 | DRI_Approach | denotes | The membrane type (MT)-matrix metalloproteinases (MMPs) constitute a subgroup of membrane-anchored MMPs that are major mediators of pericellular proteolysis and physiological activators of pro-MMP-2. |
| T2 | 384-503 | DRI_Outcome | denotes | The MT-MMPs also exhibit differential inhibition by members of the tissue inhibitor of metalloproteinase (TIMP) family. |
| T3 | 504-601 | DRI_Approach | denotes | Here we investigated the processing, catalytic activity, and TIMP inhibition of MT3-MMP (MMP-16). |
| T4 | 602-754 | DRI_Background | denotes | Inhibitor profile and mutant enzyme studies indicated that MT3-MMP is regulated on the cell surface by autocatalytic processing and ectodomain shedding. |
| T5 | 933-986 | DRI_Background | denotes | In contrast, TIMP-2 is a better inhibitor of MT1-MMP. |
| T6 | 987-1192 | DRI_Outcome | denotes | MT3-MMP requires TIMP-2 to accomplish full pro-MMP-2 activation and this process is enhanced in marimastatpretreated cells, consistent with regulation of active enzyme turnover by synthetic MMP inhibitors. |
| T7 | 1193-1272 | DRI_Outcome | denotes | TIMP-3 also enhances the activation of pro-MMP-2 by MT3-MMP but not by MT1-MMP. |
| T8 | 1273-1349 | DRI_Background | denotes | TIMP-4, in contrast, cannot support pro-MMP-2 activation with either enzyme. |
| T9 | 1350-1609 | DRI_Background | denotes | Affinity chromatography experiments demonstrated that pro-MMP-2 can assemble trimolecular complexes with a catalytic domain of MT3-MMP and TIMP-2 or TIMP-3 suggesting that pro-MMP-2 activation by MT3-MMP involves ternary complex formation on the cell surface. |
| T10 | 1610-1802 | DRI_Challenge | denotes | These results demonstrate that TIMP-3 is a major regulator of MT3-MMP activity and further underscores the unique interactions of TIMPs with MT-MMPs in the control of pericellular proteolysis. |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-183 | Sentence | denotes | Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation. |
| T2 | 184-383 | Sentence | denotes | The membrane type (MT)-matrix metalloproteinases (MMPs) constitute a subgroup of membrane-anchored MMPs that are major mediators of pericellular proteolysis and physiological activators of pro-MMP-2. |
| T3 | 384-503 | Sentence | denotes | The MT-MMPs also exhibit differential inhibition by members of the tissue inhibitor of metalloproteinase (TIMP) family. |
| T4 | 504-601 | Sentence | denotes | Here we investigated the processing, catalytic activity, and TIMP inhibition of MT3-MMP (MMP-16). |
| T5 | 602-754 | Sentence | denotes | Inhibitor profile and mutant enzyme studies indicated that MT3-MMP is regulated on the cell surface by autocatalytic processing and ectodomain shedding. |
| T6 | 755-932 | Sentence | denotes | Inhibition kinetic studies showed that TIMP-3 is a high affinity inhibitor of MT3-MMP when compared with MT1-MMP (K(i) = 0.008 nm for MT3-MMP versus K(i) = 0.16 nm for MT1-MMP). |
| T7 | 933-986 | Sentence | denotes | In contrast, TIMP-2 is a better inhibitor of MT1-MMP. |
| T8 | 987-1192 | Sentence | denotes | MT3-MMP requires TIMP-2 to accomplish full pro-MMP-2 activation and this process is enhanced in marimastatpretreated cells, consistent with regulation of active enzyme turnover by synthetic MMP inhibitors. |
| T9 | 1193-1272 | Sentence | denotes | TIMP-3 also enhances the activation of pro-MMP-2 by MT3-MMP but not by MT1-MMP. |
| T10 | 1273-1349 | Sentence | denotes | TIMP-4, in contrast, cannot support pro-MMP-2 activation with either enzyme. |
| T11 | 1350-1609 | Sentence | denotes | Affinity chromatography experiments demonstrated that pro-MMP-2 can assemble trimolecular complexes with a catalytic domain of MT3-MMP and TIMP-2 or TIMP-3 suggesting that pro-MMP-2 activation by MT3-MMP involves ternary complex formation on the cell surface. |
| T12 | 1610-1802 | Sentence | denotes | These results demonstrate that TIMP-3 is a major regulator of MT3-MMP activity and further underscores the unique interactions of TIMPs with MT-MMPs in the control of pericellular proteolysis. |
2015-BEL-Sample
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 146-754 | cat(p(HGNC:TIMP2)) decreases cat(p(HGNC:MMP14)) | denotes | TIMP-3 rgulates pro-MMP-2 activation. The membrane type (MT)-matrix metalloproteinases (MMPs) constitute a subgroup of membrane-anchored MMPs that are major mediators of pericellular proteolysis and physiological activators of pro-MMP-2. The MT-MMPs also exhibit differential inhibition by members of the tissue inhibitor of metalloproteinase (TIMP) family. Here we investigated the processing, catalytic activity, and TIMP inhibition of MT3-MMP (MMP-16). Inhibitor profile and mutant enzyme studies indicated that MT3-MMP is regulated on the cell surface by autocatalytic processing and ectodomain shedding. |
2015-BEL-Sample-2
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| BEL:20000494 | 146-754 | cat(p(HGNC:TIMP2)) decreases cat(p(HGNC:MMP14)) | denotes | TIMP-3 rgulates pro-MMP-2 activation. The membrane type (MT)-matrix metalloproteinases (MMPs) constitute a subgroup of membrane-anchored MMPs that are major mediators of pericellular proteolysis and physiological activators of pro-MMP-2. The MT-MMPs also exhibit differential inhibition by members of the tissue inhibitor of metalloproteinase (TIMP) family. Here we investigated the processing, catalytic activity, and TIMP inhibition of MT3-MMP (MMP-16). Inhibitor profile and mutant enzyme studies indicated that MT3-MMP is regulated on the cell surface by autocatalytic processing and ectodomain shedding. |
Anatomy-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 27-35 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
| T4 | 95-101 | Body_part | denotes | tissue | http://purl.obolibrary.org/obo/UBERON_0000479 |
| T5 | 188-196 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
| T8 | 265-273 | Body_part | denotes | membrane | http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158 |
| T11 | 451-457 | Body_part | denotes | tissue | http://purl.obolibrary.org/obo/UBERON_0000479 |